ID   E4V0G7_ARTGP            Unreviewed;       414 AA.
AC   E4V0G7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN   ORFNames=MGYG_06099 {ECO:0000313|EMBL:EFR03104.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; DS989826; EFR03104.1; -; Genomic_DNA.
DR   RefSeq; XP_003171558.1; XM_003171510.1.
DR   AlphaFoldDB; E4V0G7; -.
DR   STRING; 535722.E4V0G7; -.
DR   GeneID; 10026810; -.
DR   VEuPathDB; FungiDB:MGYG_06099; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   InParanoid; E4V0G7; -.
DR   OMA; GWDMQDL; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..414
FT                   /note="glucan 1,3-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003190669"
FT   DOMAIN          80..308
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          324..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45647 MW;  F2E460EEDB3F248B CRC64;
     MKFGALFGLS LVGLSVASPV SNVWKSPRGA TDDFIRGVNL GGWLVLEPWI TPGIFEEGGD
     SAVDEWTLSA ALGDRAHERL KLHWNTYIDQ GDFDRIKAAG LTHVRIPIGY WAVAPIEGEP
     FVQGQVDMLD AAVDWARHSG LKINVDLHGA PGSQNGFDNS GKLGPANWQK GNTVELTHKA
     LDVLIERYSK HEGVVDEINL INEPFPQAGI QVEPLKEFYR QGAAKVKSAN PNVAVVISDA
     FMGPSKWNGF DLGTKTIIDT HHYEVFSAEL VAWNIDQHIK AACDFGTNEL AQSSIPAVVG
     EWCGALTDCT KYLNGRHEGY RYDGTHKDSN PSTAVPNGCA RKTEGSVAQL TDEEKVNTRR
     YIEAQLDSFS KGHGWFWWTW KTQRGSPGWD LDDLLKNGLF PQPMDARMYP GQCN
//